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The FEBS Journal, ISSN 1742-464X, 02/2019, Volume 286, Issue 3, pp. 536 - 554
The rules of the genetic code are established by aminoacyl‐tRNA synthetases (aaRSs) enzymes, which covalently link tRNA with the cognate amino acid. Many aaRSs... 
protein–protein interaction | BEN1 | disulfide bond | aminoacyl‐tRNA synthetase | brassinosteroid | aminoacyl-tRNA synthetase | TRNA(SER) | BRASSINOSTEROIDS | DOMAIN | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | FLEXIBILITY | MECHANISMS | SUBSTRATE RECOGNITION | TERNARY COMPLEX | GENE | protein-protein interaction | REVEALS | Arabidopsis - enzymology | Saccharomyces cerevisiae - genetics | Substrate Specificity | Crystallography, X-Ray | Serine-tRNA Ligase - chemistry | Serine-tRNA Ligase - metabolism | Alcohol Oxidoreductases - genetics | Arabidopsis Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Serine-tRNA Ligase - genetics | Cloning, Molecular | Brassinosteroids - biosynthesis | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Arabidopsis Proteins - genetics | Gene Expression | Arabidopsis - chemistry | Genetic Vectors - chemistry | Genetic Vectors - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Alcohol Oxidoreductases - metabolism | Recombinant Proteins - genetics | Arabidopsis - genetics | Sequence Homology, Amino Acid | Two-Hybrid System Techniques | Sequence Alignment | Arabidopsis Proteins - chemistry | Protein Conformation, beta-Strand | Alcohol Oxidoreductases - chemistry | Protein Binding | Kinetics | Arabidopsis thaliana | Crystals | Physiological aspects | Aminoacyl-tRNA synthetases | Structure | Protein-protein interactions | Transfer RNA | Protein binding | Translation | Disulfide bonds | Aminoacylation | Yeast | tRNA | Amino acids | Hormones | Metabolism | Crystallography | Protein turnover | Proteins | Genetic code | Metabolic pathways | Catalysis | Protein structure | Crystal structure
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 03/2013, Volume 5, Issue 3, pp. 332 - 343
Aminoacyl‐tRNA synthetases (ARSs) are essential and ubiquitous ‘house‐keeping’ enzymes responsible for charging amino acids to their cognate tRNAs and... 
therapeutics | tRNA | human disease | aminoacyl‐tRNA synthetases (ARSs) | Aminoacyl-tRNA synthetases (ARSs) | Human disease | TRNA | Therapeutics | ANTIFUNGAL AGENT | MEDICINE, RESEARCH & EXPERIMENTAL | aminoacyl-tRNA synthetases (ARSs) | BRAIN-STEM | NONCANONICAL FUNCTION | PROTEIN-SYNTHESIS | LEUKOENCEPHALOPATHY | GENE | CAUSES MYOPATHY | LACTIC-ACIDOSIS | MUTATIONS | SPINAL-CORD INVOLVEMENT | Aminoacylation | Charcot-Marie-Tooth Disease - enzymology | Humans | Fungal Proteins - antagonists & inhibitors | Antifungal Agents - therapeutic use | Charcot-Marie-Tooth Disease - genetics | Anti-Bacterial Agents - therapeutic use | Amino Acyl-tRNA Synthetases - metabolism | Amino Acyl-tRNA Synthetases - genetics | Mitochondrial Diseases - genetics | Bacterial Proteins - antagonists & inhibitors | Enzyme Replacement Therapy | Mitochondrial Diseases - drug therapy | Genetic Predisposition to Disease | Gene Expression Regulation | Charcot-Marie-Tooth Disease - drug therapy | Mitochondrial Diseases - enzymology | Amino Acyl-tRNA Synthetases - therapeutic use | Phenotype | Animals | Bacterial Proteins - metabolism | Protein Biosynthesis - drug effects | Mutation | Amino Acyl-tRNA Synthetases - antagonists & inhibitors | Fungal Proteins - metabolism | Aminoacyl-tRNA synthetases | Protein biosynthesis | Transfer RNA | Heart | Enzymes | Editing | Cardiovascular disease | Amino acids | Mammals | Hearing impairment | Peripheral neuropathy | Cell adhesion & migration | Proteins | Signal transduction | Angiogenesis | Genotype & phenotype | Antibiotics | Protein synthesis | Etiology | Ataxia | Autoimmune diseases | Reviews
Journal Article
Journal Article
Nature Reviews Molecular Cell Biology, ISSN 1471-0072, 09/2010, Volume 11, Issue 9, pp. 668 - 674
Journal Article